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Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58
dc.contributor.author | Martínez Rodríguez, Sergio | |
dc.contributor.author | Las Heras Vázquez, Francisco Javier | |
dc.contributor.author | Clemente Jiménez, Josefa María | |
dc.contributor.author | Rodríguez Vico, Felipe | |
dc.date.accessioned | 2024-05-23T10:22:02Z | |
dc.date.available | 2024-05-23T10:22:02Z | |
dc.date.issued | 2004 | |
dc.identifier.issn | 0300-9084 | |
dc.identifier.uri | http://hdl.handle.net/10835/16558 | |
dc.description.abstract | A novel hydantoin racemase gene of Agrobacterium tumefaciens C58 (AthyuA2) has been cloned and expressed in Escherichia coli BL21. The recombinant protein was purified in a one-step procedure and showed an apparent molecular mass of 27,000 Da in SDS-gel electrophoresis. Size exclusion chromatography analysis determined a molecular mass of approximately 100,000 Da, suggesting that the native enzyme is a tetramer. The optimum pH and temperature for hydantoin racemase activity were 7.5 and 55 °C, respectively, with L-5-ethylhydantoin as substrate. Enzyme activity was strongly inhibited by Cu2+ and Hg2+. No effect on enzyme activity was detected with any other divalent cations, EDTA or DTT, suggesting that it is not a metalloenzyme. Kinetic studies showed the preference of the enzyme for hydantoins with short rather than long aliphatic side chains or hydantoins with aromatic rings. | es_ES |
dc.language.iso | en | es_ES |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Racemization | es_ES |
dc.subject | D-amino acid | es_ES |
dc.subject | Hydantoin racemase 2 | es_ES |
dc.subject | Purification | es_ES |
dc.title | Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58 | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es_ES |